% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@MISC{Kroon:282939,
      author       = {Kroon, Cristina and Nagy-Herczeg, Domonkos and Aguilar
                      Perez, Gerard and Ranti, Dimitra and Syropoulou, Vasiliki},
      title        = {{D}ataset: {P}hosphorylation of presynaptic {PLPPR}3
                      controls synaptic vesicle release},
      publisher    = {Mendeley Data},
      reportid     = {DZNE-2025-01400},
      year         = {2025},
      abstract     = {This dataset contains the raw data from the publication
                      „Phosphorylation of presynaptic PLPPR3 controls synaptic
                      vesicle release“ Kroon et al. 2025 published in iScience.
                      Presented here are the original western and PhosTag blots
                      supporting the biochemical characterization, as well as mass
                      spectrometry and immunocytochemistry data. For further
                      details please refer to the publication. Abstract:
                      Phospholipid-phosphatase related protein 3 (PLPPR3) belongs
                      to a family of transmembrane proteins highly expressed in
                      the nervous system where it regulates critical axonal growth
                      processes during guidance, filopodia formation and
                      branching. However, little is known regarding its role in
                      synapses and the signaling events regulating PLPPR3
                      function. Here, we identify 26 high-confidence
                      phosphorylation sites in the intracellular domain of PLPPR3
                      using mass spectrometry. Biochemical characterization
                      established one of these – S351 – as a bona fide
                      phosphorylation site of protein kinase A (PKA). PLPPR3 is
                      enriched at presynaptic terminals, and deletion of PLPPR3
                      results in increased depolarization-induced synaptic vesicle
                      release in hippocampal neurons. This tonic inhibitory signal
                      towards depolarization-induced presynaptic activity is
                      corrected by expression of PLPPR3 intracellular domain, but
                      not a S351A phospho-dead mutant, in Plppr3-/- hippocampal
                      neurons. We propose that a PLPPR3 phosphorylation under the
                      control of PKA activity is a novel signaling integrator of
                      presynaptic activity in hippocampal neurons.},
      keywords     = {Molecular Neuroscience (Other) / Phosphorylation (Other) /
                      Protein-Protein Interaction (Other) / Signal Transduction
                      (Other) / Cellular Neuroscience (Other) / Presynaptic
                      Mechanisms of Synaptic Transmission (Other) / Protein
                      Phosphorylation (Other)},
      cin          = {AG Milovanovic (Berlin)},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)32},
      doi          = {10.17632/w97nrdvxbc.1},
      url          = {https://pub.dzne.de/record/282939},
}